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Protein

Nuclear RNA export factor 1

Gene

NXF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex. ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export.3 Publications

GO - Molecular functioni

  • mRNA binding Source: Ensembl
  • nucleocytoplasmic transporter activity Source: Ensembl
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • single-stranded RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
SIGNORiQ9UBU9.

Protein family/group databases

TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear RNA export factor 1
Alternative name(s):
Tip-associated protein
Tip-associating protein
mRNA export factor TAP
Gene namesi
Name:NXF1
Synonyms:TAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:8071. NXF1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • nuclear inclusion body Source: Ensembl
  • nuclear pore Source: Ensembl
  • nuclear speck Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi71 – 711R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-78, A-81, A-82, A-89, A-91, A-97, A-98, A-100 and A-105. 1 Publication
Mutagenesisi78 – 781R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-81, A-82, A-89, A-91, A-97, A-98, A-100 and A-105. 1 Publication
Mutagenesisi81 – 811R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-82, A-89, A-91, A-97, A-98, A-100 and A-105. 1 Publication
Mutagenesisi82 – 821R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-89, A-91, A-97, A-98, A-100 and A-105. 1 Publication
Mutagenesisi89 – 891R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-91, A-97, A-98, A-100 and A-105. 1 Publication
Mutagenesisi91 – 911R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-97, A-98, A-100 and A-105. 1 Publication
Mutagenesisi97 – 971R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-98, A-100 and A-105. 1 Publication
Mutagenesisi98 – 981R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-97, A-100 and A-105. 1 Publication
Mutagenesisi100 – 1001R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-97, A-98 and A-105. 1 Publication
Mutagenesisi105 – 1051R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-97, A-98 and A-100. 1 Publication
Mutagenesisi306 – 3083ERE → AAA: Decreases the export of mRNAs from the nucleus.
Mutagenesisi383 – 3831L → R: Diminishes nuclear rim staining and 80% reduction in mRNA export activity; when associated with R-386. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-386 and A-594. 1 Publication
Mutagenesisi386 – 3861L → R: Diminishes nuclear rim staining and 80% reduction in mRNA export activity; when associated with R-383. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-383 and A-594. 1 Publication
Mutagenesisi399 – 3991D → A: 60% reduction in mRNA export activity. 1 Publication
Mutagenesisi450 – 4534LRFR → AAAA: Abolishes interaction with THOC5 and CHTOP. 1 Publication
Mutagenesisi453 – 4531R → A: Impairs intramolecular interaction between RBD and NTF2. 1 Publication
Mutagenesisi456 – 4594KHTR → AAAA: Abolishes interaction with THOC5 and CHTOP, no effect on interaction with NXT1; enhances intramolecular interaction between RBD and NTF2, reduces RNA binding and mRNA export. 2 Publications
Mutagenesisi456 – 4561K → D: Impairs intramolecular interaction between RBD and NTF2; when associated with D-459.
Mutagenesisi459 – 4591R → D: Impairs intramolecular interaction between RBD and NTF2; when associated with D-456.
Mutagenesisi482 – 4821D → R: 90% reduction in mRNA export activity. 1 Publication
Mutagenesisi518 – 5181I → R: 98% reduction in mRNA export activity. 1 Publication
Mutagenesisi521 – 5211P → Q: 35% reduction in mRNA export activity. 1 Publication
Mutagenesisi594 – 5941W → A: Suppresses FG-nucleoporin binding. Diminishes nuclear rim staining and 88% reduction in mRNA export activity. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-383 and R-386. 1 Publication
Mutagenesisi595 – 5951D → R: Suppresses FG-nucleoporin binding.
Mutagenesisi617 – 6171F → A: Suppresses FG-nucleoporin binding. 1 Publication

Organism-specific databases

PharmGKBiPA31858.

Polymorphism and mutation databases

BioMutaiNXF1.
DMDMi20139282.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 619618Nuclear RNA export factor 1PRO_0000220529Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei9 – 91PhosphoserineCombined sources
Modified residuei126 – 1261Nitrated tyrosineBy similarity

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

EPDiQ9UBU9.
MaxQBiQ9UBU9.
PaxDbiQ9UBU9.
PeptideAtlasiQ9UBU9.
PRIDEiQ9UBU9.

PTM databases

iPTMnetiQ9UBU9.
PhosphoSiteiQ9UBU9.

Expressioni

Tissue specificityi

Expressed ubiquitously.

Gene expression databases

BgeeiENSG00000162231.
CleanExiHS_NXF1.
ExpressionAtlasiQ9UBU9. baseline and differential.
GenevisibleiQ9UBU9. HS.

Organism-specific databases

HPAiCAB016327.
HPA061593.
HPA064429.

Interactioni

Subunit structurei

Heterodimer with NXT1 (PubMed:11583626). The formation of NXF1-NXT1 heterodimers is required for the NXF1-mediated nuclear mRNA export (PubMed:11583626). Found in a post-splicing complex with RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1 (PubMed:11546874). Interacts (via NTF2 domain) with NXT1 (PubMed:11583626). Interacts with ALYREF/THOC4 (PubMed:11707413, PubMed:14730019, PubMed:19165146, PubMed:23299939). Interacts with FYTTD1/UIF (PubMed:19836239). Interacts with EIF4A3 (PubMed:14730019). Interacts with NUPL2 (PubMed:10228171). Interacts with THOC5 (PubMed:19165146, PubMed:23299939). Interacts with CHTOP (PubMed:23299939, PubMed:23826332). Interacts with FRG1 (via N-terminus) (PubMed:21699900). Interacts with LUZP4 (PubMed:25662211). Interacts with FMR1; the interaction occurs in a mRNA-dependent and polyribosomes-independent manner in the nucleus (PubMed:18936162). Associates with the exon junction complex (EJC) and with the transcription/export (TREX) complex (PubMed:11707413, PubMed:22893130). Found in a mRNA complex with UPF3A and UPF3B (PubMed:11546873).17 Publications
(Microbial infection) Interacts with Saimiriine herpesvirus 2 TIP protein.1 Publication
(Microbial infection) Interacts with human herpes virus 1 (HHV-1) ICP27 protein; this interaction allows efficient export of HHV-1 early and late transcripts.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
P225756EBI-398874,EBI-866709From a different organism.
ALYREFQ86V814EBI-398874,EBI-347640
CHTOPQ9Y3Y29EBI-398874,EBI-347794
DDX3XO005715EBI-398874,EBI-353779
DHX9Q082118EBI-398874,EBI-352022
DVL3Q929973EBI-398874,EBI-739789
GFAPP141363EBI-398874,EBI-744302
KRT40Q6A1623EBI-398874,EBI-10171697
LDOC1O957513EBI-398874,EBI-740738
MID2Q9UJV3-23EBI-398874,EBI-10172526
NUP62P371986EBI-398874,EBI-347978
NXT1Q9UKK65EBI-398874,EBI-301889
SRSF1Q079555EBI-398874,EBI-398920
SRSF3P841034EBI-398874,EBI-372557
SRSF7Q166294EBI-398874,EBI-398885
THRAP3Q9Y2W14EBI-398874,EBI-352039
TIFAQ96CG33EBI-398874,EBI-740711
TP53BP2Q13625-33EBI-398874,EBI-10175039
UL54P102384EBI-398874,EBI-6883946From a different organism.

Protein-protein interaction databases

BioGridi115745. 1130 interactions.
DIPiDIP-31789N.
IntActiQ9UBU9. 78 interactions.
MINTiMINT-121360.
STRINGi9606.ENSP00000294172.

Structurei

Secondary structure

1
619
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi120 – 1245Combined sources
Helixi127 – 1293Combined sources
Helixi132 – 14110Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi150 – 1556Combined sources
Beta strandi158 – 1647Combined sources
Helixi166 – 1749Combined sources
Turni176 – 1783Combined sources
Beta strandi190 – 1934Combined sources
Helixi198 – 2014Combined sources
Helixi206 – 21813Combined sources
Turni222 – 2254Combined sources
Beta strandi226 – 2283Combined sources
Helixi232 – 2343Combined sources
Helixi236 – 2405Combined sources
Helixi250 – 26314Combined sources
Beta strandi269 – 2713Combined sources
Helixi281 – 2855Combined sources
Helixi286 – 2894Combined sources
Beta strandi295 – 2973Combined sources
Helixi306 – 3127Combined sources
Beta strandi318 – 3214Combined sources
Helixi328 – 3303Combined sources
Helixi334 – 34411Combined sources
Beta strandi350 – 3534Combined sources
Helixi381 – 39818Combined sources
Helixi403 – 4086Combined sources
Beta strandi410 – 41910Combined sources
Helixi433 – 4364Combined sources
Turni442 – 4443Combined sources
Helixi448 – 4547Combined sources
Beta strandi455 – 4584Combined sources
Helixi459 – 4668Combined sources
Beta strandi472 – 4743Combined sources
Helixi476 – 4783Combined sources
Beta strandi480 – 4867Combined sources
Beta strandi491 – 50111Combined sources
Turni505 – 5084Combined sources
Beta strandi510 – 52112Combined sources
Beta strandi525 – 53814Combined sources
Helixi541 – 5488Combined sources
Beta strandi553 – 5575Combined sources
Helixi565 – 57814Combined sources
Helixi582 – 59110Combined sources
Turni592 – 5943Combined sources
Helixi596 – 60813Combined sources
Helixi614 – 6174Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FO1X-ray2.90A/B102-372[»]
1FT8X-ray3.15A/B/C/D/E102-372[»]
1GO5NMR-A551-619[»]
1JKGX-ray1.90B371-619[»]
1JN5X-ray2.80B371-619[»]
1KOHX-ray3.80A/B/C/D96-372[»]
1KOOX-ray3.80A/B/C/D96-372[»]
1OAIX-ray1.00A561-619[»]
2Z5KX-ray2.60B53-82[»]
2Z5MX-ray3.00B53-82[»]
3RW6X-ray2.30A/B96-362[»]
3RW7X-ray3.00A/B/C/D96-362[»]
4WYKX-ray3.40A/C96-555[»]
ProteinModelPortaliQ9UBU9.
SMRiQ9UBU9. Positions 118-549, 551-619.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UBU9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini119 – 19880RRMAdd
BLAST
Repeati266 – 29126LRR 1Add
BLAST
Repeati292 – 31524LRR 2Add
BLAST
Repeati316 – 34328LRR 3Add
BLAST
Repeati344 – 37128LRR 4Add
BLAST
Domaini386 – 536151NTF2PROSITE-ProRule annotationAdd
BLAST
Domaini565 – 61955TAP-CPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 198197Interaction with ALYREF/THOC4 and LUZP41 PublicationAdd
BLAST
Regioni2 – 118117RNA-binding (RBD)Add
BLAST
Regioni2 – 6059Minor non-specific RNA-bindingAdd
BLAST
Regioni61 – 11858Major non-specific RNA-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi67 – 10034Nuclear localization signalAdd
BLAST
Motifi83 – 11028Nuclear export signalAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi551 – 56111Pro-richAdd
BLAST

Domaini

The minimal CTE binding domain consists of an RNP-type RNA binding domain (RBD) and leucine-rich repeats.1 Publication
The nucleoporin binding domain consists of a NTF2 domain (also called NTF2-like domain) and a TAP-C domain (also called UBA-like domain). It has 2 nucleoporin-FG-repeats binding sites (one in the NTF2 and the other in the TAP-C domain) which contribute to nucleoporin association and act synergistically to export cellular mRNAs.1 Publication
The NTF2 domain is functional only in the presence of NXT1 and is essential for the export of mRNA from the nucleus. It inhibits RNA binding activity through an intramolecular interaction with the N-terminal RNA binding domain (RBD); the inhibition is removed by an association with the TREX complex, specifically involving ALYREF/THOC4 and THOC5.1 Publication
The TAP-C domain mediates direct interactions with nucleoporin-FG-repeats and is necessary and sufficient for localization of NXF1 to the nuclear rim. The conserved loop 594-NWD-596 of the TAP-C domain has a critical role in the interaction with nucleoporins.1 Publication
The leucine-rich repeats are essential for the export of mRNA from the nucleus.1 Publication
The RNA-binding domain is a non-canonical RNP-type domain.1 Publication

Sequence similaritiesi

Belongs to the NXF family.Curated
Contains 4 LRR (leucine-rich) repeats.Curated
Contains 1 NTF2 domain.PROSITE-ProRule annotation
Contains 1 TAP-C domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG3763. Eukaryota.
ENOG410XR55. LUCA.
GeneTreeiENSGT00390000007539.
HOGENOMiHOG000236269.
HOVERGENiHBG013199.
InParanoidiQ9UBU9.
KOiK14284.
OMAiYAVYDSG.
OrthoDBiEOG091G04QA.
PhylomeDBiQ9UBU9.
TreeFamiTF314566.

Family and domain databases

CDDicd00780. NTF2. 1 hit.
cd14342. UBA_TAP-C. 1 hit.
Gene3Di3.10.450.50. 1 hit.
3.30.70.330. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR002075. NTF2.
IPR032710. NTF2-like_dom.
IPR018222. Nuclear_transport_factor_2_euk.
IPR012677. Nucleotide-bd_a/b_plait.
IPR005637. TAP_C_dom.
IPR015245. Tap_RNA-bd.
IPR009060. UBA-like.
[Graphical view]
PfamiPF02136. NTF2. 1 hit.
PF09162. Tap-RNA_bind. 1 hit.
PF03943. TAP_C. 1 hit.
[Graphical view]
ProDomiPD043466. Tap_RNA_bd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00804. TAP_C. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF52058. SSF52058. 1 hit.
SSF54427. SSF54427. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS51450. LRR. 3 hits.
PS50177. NTF2_DOMAIN. 1 hit.
PS51281. TAP_C. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UBU9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADEGKSYSE HDDERVNFPQ RKKKGRGPFR WKYGEGNRRS GRGGSGIRSS
60 70 80 90 100
RLEEDDGDVA MSDAQDGPRV RYNPYTTRPN RRGDTWHDRD RIHVTVRRDR
110 120 130 140 150
APPERGGAGT SQDGTSKNWF KITIPYGRKY DKAWLLSMIQ SKCSVPFTPI
160 170 180 190 200
EFHYENTRAQ FFVEDASTAS ALKAVNYKIL DRENRRISII INSSAPPHTI
210 220 230 240 250
LNELKPEQVE QLKLIMSKRY DGSQQALDLK GLRSDPDLVA QNIDVVLNRR
260 270 280 290 300
SCMAATLRII EENIPELLSL NLSNNRLYRL DDMSSIVQKA PNLKILNLSG
310 320 330 340 350
NELKSERELD KIKGLKLEEL WLDGNSLCDT FRDQSTYISA IRERFPKLLR
360 370 380 390 400
LDGHELPPPI AFDVEAPTTL PPCKGSYFGT ENLKSLVLHF LQQYYAIYDS
410 420 430 440 450
GDRQGLLDAY HDGACCSLSI PFIPQNPARS SLAEYFKDSR NVKKLKDPTL
460 470 480 490 500
RFRLLKHTRL NVVAFLNELP KTQHDVNSFV VDISAQTSTL LCFSVNGVFK
510 520 530 540 550
EVDGKSRDSL RAFTRTFIAV PASNSGLCIV NDELFVRNAS SEEIQRAFAM
560 570 580 590 600
PAPTPSSSPV PTLSPEQQEM LQAFSTQSGM NLEWSQKCLQ DNNWDYTRSA
610
QAFTHLKAKG EIPEVAFMK
Length:619
Mass (Da):70,182
Last modified:May 1, 2000 - v1
Checksum:i338872AADA789FBF
GO
Isoform 2 (identifier: Q9UBU9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     339-356: SAIRERFPKLLRLDGHEL → RSVVACVSPPGDLHPLGG
     357-619: Missing.

Show »
Length:356
Mass (Da):40,476
Checksum:i470701F5324EC0B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191W → C in AAB81111 (PubMed:9175835).Curated
Sequence conflicti256 – 2561T → N in AAD20016 (PubMed:10454577).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei339 – 35618SAIRE…DGHEL → RSVVACVSPPGDLHPLGG in isoform 2. 1 PublicationVSP_041427Add
BLAST
Alternative sequencei357 – 619263Missing in isoform 2. 1 PublicationVSP_041428Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132712 mRNA. Translation: CAA10753.1.
AF112880 mRNA. Translation: AAD39102.1.
AF126246 mRNA. Translation: AAD20016.1.
AK304137 mRNA. Translation: BAG65031.1.
AK027192 mRNA. No translation available.
AP001160 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74105.1.
BC004904 mRNA. Translation: AAH04904.1.
BC028041 mRNA. Translation: AAH28041.1.
U80073 mRNA. Translation: AAB81111.1.
CCDSiCCDS44629.1. [Q9UBU9-2]
CCDS8037.1. [Q9UBU9-1]
RefSeqiNP_001074960.1. NM_001081491.1. [Q9UBU9-2]
NP_006353.2. NM_006362.4. [Q9UBU9-1]
UniGeneiHs.523739.
Hs.601546.

Genome annotation databases

EnsembliENST00000294172; ENSP00000294172; ENSG00000162231. [Q9UBU9-1]
ENST00000531709; ENSP00000453885; ENSG00000162231. [Q9UBU9-2]
ENST00000532297; ENSP00000436679; ENSG00000162231. [Q9UBU9-1]
GeneIDi10482.
KEGGihsa:10482.
UCSCiuc001nvf.1. human. [Q9UBU9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132712 mRNA. Translation: CAA10753.1.
AF112880 mRNA. Translation: AAD39102.1.
AF126246 mRNA. Translation: AAD20016.1.
AK304137 mRNA. Translation: BAG65031.1.
AK027192 mRNA. No translation available.
AP001160 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74105.1.
BC004904 mRNA. Translation: AAH04904.1.
BC028041 mRNA. Translation: AAH28041.1.
U80073 mRNA. Translation: AAB81111.1.
CCDSiCCDS44629.1. [Q9UBU9-2]
CCDS8037.1. [Q9UBU9-1]
RefSeqiNP_001074960.1. NM_001081491.1. [Q9UBU9-2]
NP_006353.2. NM_006362.4. [Q9UBU9-1]
UniGeneiHs.523739.
Hs.601546.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FO1X-ray2.90A/B102-372[»]
1FT8X-ray3.15A/B/C/D/E102-372[»]
1GO5NMR-A551-619[»]
1JKGX-ray1.90B371-619[»]
1JN5X-ray2.80B371-619[»]
1KOHX-ray3.80A/B/C/D96-372[»]
1KOOX-ray3.80A/B/C/D96-372[»]
1OAIX-ray1.00A561-619[»]
2Z5KX-ray2.60B53-82[»]
2Z5MX-ray3.00B53-82[»]
3RW6X-ray2.30A/B96-362[»]
3RW7X-ray3.00A/B/C/D96-362[»]
4WYKX-ray3.40A/C96-555[»]
ProteinModelPortaliQ9UBU9.
SMRiQ9UBU9. Positions 118-549, 551-619.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115745. 1130 interactions.
DIPiDIP-31789N.
IntActiQ9UBU9. 78 interactions.
MINTiMINT-121360.
STRINGi9606.ENSP00000294172.

Protein family/group databases

TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

iPTMnetiQ9UBU9.
PhosphoSiteiQ9UBU9.

Polymorphism and mutation databases

BioMutaiNXF1.
DMDMi20139282.

Proteomic databases

EPDiQ9UBU9.
MaxQBiQ9UBU9.
PaxDbiQ9UBU9.
PeptideAtlasiQ9UBU9.
PRIDEiQ9UBU9.

Protocols and materials databases

DNASUi10482.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294172; ENSP00000294172; ENSG00000162231. [Q9UBU9-1]
ENST00000531709; ENSP00000453885; ENSG00000162231. [Q9UBU9-2]
ENST00000532297; ENSP00000436679; ENSG00000162231. [Q9UBU9-1]
GeneIDi10482.
KEGGihsa:10482.
UCSCiuc001nvf.1. human. [Q9UBU9-1]

Organism-specific databases

CTDi10482.
GeneCardsiNXF1.
HGNCiHGNC:8071. NXF1.
HPAiCAB016327.
HPA061593.
HPA064429.
MIMi602647. gene.
neXtProtiNX_Q9UBU9.
PharmGKBiPA31858.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3763. Eukaryota.
ENOG410XR55. LUCA.
GeneTreeiENSGT00390000007539.
HOGENOMiHOG000236269.
HOVERGENiHBG013199.
InParanoidiQ9UBU9.
KOiK14284.
OMAiYAVYDSG.
OrthoDBiEOG091G04QA.
PhylomeDBiQ9UBU9.
TreeFamiTF314566.

Enzyme and pathway databases

ReactomeiR-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
SIGNORiQ9UBU9.

Miscellaneous databases

ChiTaRSiNXF1. human.
EvolutionaryTraceiQ9UBU9.
GeneWikiiNXF1.
GenomeRNAii10482.
PROiQ9UBU9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000162231.
CleanExiHS_NXF1.
ExpressionAtlasiQ9UBU9. baseline and differential.
GenevisibleiQ9UBU9. HS.

Family and domain databases

CDDicd00780. NTF2. 1 hit.
cd14342. UBA_TAP-C. 1 hit.
Gene3Di3.10.450.50. 1 hit.
3.30.70.330. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR002075. NTF2.
IPR032710. NTF2-like_dom.
IPR018222. Nuclear_transport_factor_2_euk.
IPR012677. Nucleotide-bd_a/b_plait.
IPR005637. TAP_C_dom.
IPR015245. Tap_RNA-bd.
IPR009060. UBA-like.
[Graphical view]
PfamiPF02136. NTF2. 1 hit.
PF09162. Tap-RNA_bind. 1 hit.
PF03943. TAP_C. 1 hit.
[Graphical view]
ProDomiPD043466. Tap_RNA_bd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00804. TAP_C. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF52058. SSF52058. 1 hit.
SSF54427. SSF54427. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS51450. LRR. 3 hits.
PS50177. NTF2_DOMAIN. 1 hit.
PS51281. TAP_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNXF1_HUMAN
AccessioniPrimary (citable) accession number: Q9UBU9
Secondary accession number(s): B4E269, Q99799, Q9UQL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 183 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.